scholarly journals JAMP, a Jun N-Terminal Kinase 1 (JNK1)-Associated Membrane Protein, Regulates Duration of JNK Activity

2005 ◽  
Vol 25 (19) ◽  
pp. 8619-8630 ◽  
Author(s):  
Takayuki Kadoya ◽  
Ashwani Khurana ◽  
Marianna Tcherpakov ◽  
Kenneth D. Bromberg ◽  
Christine Didier ◽  
...  
Keyword(s):  
Transmembrane Protein ◽  
Mitogen Activated Protein Kinase ◽  
Treatment Results ◽  
Apoptosis Inhibition ◽  
Mitogen Activated Protein ◽  
Elevated Expression ◽  
Induced Apoptosis ◽  
Jnk Activation ◽  
Identification And Characterization

ABSTRACT We report the identification and characterization of JAMP (JNK1 [Jun N-terminal kinase 1]-associated membrane protein), a predicted seven-transmembrane protein that is localized primarily within the plasma membrane and associates with JNK1 through its C-terminal domain. JAMP association with JNK1 outcompetes JNK1 association with mitogen-activated protein kinase phosphatase 5, resulting in increased and prolonged JNK1 activity following stress. Elevated expression of JAMP following UV or tunicamycin treatment results in sustained JNK activity and a higher level of JNK-dependent apoptosis. Inhibition of JAMP expression by RNA interference reduces the degree and duration of JNK activation and concomitantly the level of stress-induced apoptosis. Through its regulation of JNK1 activity, JAMP emerges as a membrane-anchored regulator of the duration of JNK1 activity in response to diverse stress stimuli.

Self-incompatibility in Papaver: identification of the pollen S-determinant PrpS

2010 ◽  
Vol 38 (2) ◽  
pp. 588-592 ◽  
Author(s):  
Natalie S. Poulter ◽  
Michael J. Wheeler ◽  
Maurice Bosch ◽  
Vernonica E. Franklin-Tong
Keyword(s):  
Transmembrane Protein ◽  
Mitogen Activated Protein Kinase ◽  
Self Incompatibility ◽  
Incompatible Pollen ◽  
Signalling Network ◽  
Mitogen Activated Protein ◽  
Significant Step ◽  
Self Fertilization ◽  
Subsequent Loss

Many flowering plants are hermaphrodite, posing the problem of self-fertilization and the subsequent loss of the genetic fitness of the offspring. To prevent this, many plants have developed a genetically controlled mechanism called self-incompatibility (SI). When the male and female S-determinants match, self (incompatible) pollen is recognized and rejected before fertilization can occur. In poppy (Papaver rhoeas), the pistil S-determinant (PrsS) is a small secreted protein that interacts with incompatible pollen, initiating a Ca2+-dependent signalling network. SI triggers several downstream events, including depolymerization of the cytoskeleton, phosphorylation of two soluble inorganic pyrophosphatases and an MAPK (mitogen-activated protein kinase). This culminates in PCD (programmed cell death) involving several caspase-like activities. The recent discovery of the Papaver pollen S-determinant PrpS marks a significant step forward in the understanding of the Papaver SI system. PrpS encodes a ~20 kDa predicted transmembrane protein which has no homology with known proteins. It is specifically expressed in pollen, linked to the pistil S-determinant, and displays the high polymorphism expected of an S-locus determinant. The present review focuses on the discovery and characterization of PrpS which strongly support the hypothesis that Papaver SI is triggered by the interaction of PrsS and PrpS.

scholarly journals Identification and Characterization of Mitogen-Activated Protein Kinase (MAPK) Genes in Sunflower (Helianthus annuus L.)

Plants ◽  
2019 ◽  
Vol 8 (2) ◽  
pp. 28 ◽  
Author(s):  
Surendra Neupane ◽  
Sarah Schweitzer ◽  
Achal Neupane ◽  
Ethan Andersen ◽  
Anne Fennell ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Helianthus Annuus ◽  
Plant Species ◽  
Crop Improvement ◽  
Mitogen Activated Protein Kinase ◽  
Plant Kingdom ◽  
Mitogen Activated Protein ◽  
Identification And Characterization

Mitogen-Activated Protein Kinase (MAPK) genes encode proteins that regulate biotic and abiotic stresses in plants through signaling cascades comprised of three major subfamilies: MAP Kinase (MPK), MAPK Kinase (MKK), and MAPKK Kinase (MKKK). The main objectives of this research were to conduct genome-wide identification of MAPK genes in Helianthus annuus and examine functional divergence of these genes in relation to those in nine other plant species (Amborella trichopoda, Aquilegia coerulea, Arabidopsis thaliana, Daucus carota, Glycine max, Oryza sativa, Solanum lycopersicum, Sphagnum fallax, and Vitis vinifera), representing diverse taxonomic groups of the Plant Kingdom. A Hidden Markov Model (HMM) profile of the MAPK genes utilized reference sequences from A. thaliana and G. max, yielding a total of 96 MPKs and 37 MKKs in the genomes of A. trichopoda, A. coerulea, C. reinhardtii, D. carota, H. annuus, S. lycopersicum, and S. fallax. Among them, 28 MPKs and eight MKKs were confirmed in H. annuus. Phylogenetic analyses revealed four clades within each subfamily. Transcriptomic analyses showed that at least 19 HaMPK and seven HaMKK genes were induced in response to salicylic acid (SA), sodium chloride (NaCl), and polyethylene glycol (Peg) in leaves and roots. Of the seven published sunflower microRNAs, five microRNA families are involved in targeting eight MPKs. Additionally, we discussed the need for using MAP Kinase nomenclature guidelines across plant species. Our identification and characterization of MAP Kinase genes would have implications in sunflower crop improvement, and in advancing our knowledge of the diversity and evolution of MAPK genes in the Plant Kingdom.

scholarly journals Phospholipase D Elevates the Level of MDM2 and Suppresses DNA Damage-Induced Increases in p53

2004 ◽  
Vol 24 (13) ◽  
pp. 5677-5686 ◽  
Author(s):  
Li Hui ◽  
Tarek Abbas ◽  
Rafal M. Pielak ◽  
Troy Joseph ◽  
Jill Bargonetti ◽  
...  
Keyword(s):  
Dna Damage ◽  
Phospholipase D ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Mdm2 Expression ◽  
Elevated Expression ◽  
P53 Response ◽  
P53 Activation ◽  
Induced Apoptosis ◽  
Survival Signals

ABSTRACT Phospholipase D (PLD) has been reported to generate survival signals that prevent apoptosis induced by serum withdrawal. We have now found that elevated expression of PLD also suppresses DNA damage-induced apoptosis. Since DNA damage-induced apoptosis is often mediated by p53, we examined the effect of elevated PLD expression on the regulation of p53 stabilization. We report here that PLD suppresses DNA damage-induced increases in p53 stabilization in cells where PLD has been shown to provide a survival signal. Elevated expression of PLD also led to increased expression of the p53 E3 ubiquitin ligase MDM2 and increased turnover of p53. PLD1-stimulated increases in MDM2 expression and suppression of p53 activation were blocked by inhibition of mTOR and the mitogen-activated protein kinase pathway. Although PLD did not activate the phosphatidylinositol 3-kinase (PI3K)/Akt survival pathway activate the basal levels of PI3K activity were partially required for PLD1-induced increases in MDM2. These data provide evidence that survival signals generated by PLD involve suppression of the p53 response pathway.

scholarly journals Zamzam water protects cancer cells from chemotherapy-induced apoptosis via mitogen-activated protein kinase-dependent pathway

2019 ◽  
Vol 118 ◽  
pp. 109376
Author(s):  
Abdul Khalid Siraj ◽  
Rafia Begum ◽  
Roxanne Melosantos ◽  
Wafaa Albalawy ◽  
Jehan Abboud ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cancer Cells ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Induced Apoptosis ◽  
Dependent Pathway

scholarly journals UVB-mediated activation of p38 mitogen-activated protein kinase enhances resistance of normal human keratinocytes to apoptosis by stabilizing cytoplasmic p53

2002 ◽  
Vol 365 (1) ◽  
pp. 133-145 ◽  
Author(s):  
Nadine CHOUINARD ◽  
Kristoffer VALERIE ◽  
Mahmoud ROUABHIA ◽  
Jacques HUOT
Keyword(s):  
Adaptive Response ◽  
Human Keratinocytes ◽  
Dominant Negative ◽  
Mitogen Activated Protein Kinase ◽  
Dominant Negative Mutant ◽  
Normal Human Keratinocytes ◽  
Mitogen Activated Protein ◽  
Normal Human ◽  
Induced Apoptosis ◽  
Negative Mutant

Human keratinocytes respond to UV rays by developing a fast adaptive response that contributes to maintaining their functions and survival. We investigated the role of the mitogen-activated protein kinase pathways in transducing the UV signals in normal human keratinocytes. We found that UVA, UVB or UVC induced a marked and persistent activation of p38, whereas c-Jun N-terminal kinase or extracellular signal-regulated kinase were less or not activated respectively. Inhibition of p38 activity by expression of a dominant-negative mutant of p38 or with SB203580 impaired cell viability and led to an increase in UVB-induced apoptosis. This sensitization to apoptosis was independent of caspase activities. Inhibition of p38 did not sensitize transformed HaCaT keratinocytes to UVB-induced apoptosis. In normal keratinocytes, expression of a dominant-negative mutant of p53 increased UVB-induced cell death, pointing to a role for p53. In these cells, UVB triggered a p38-dependent phosphorylation of p53 on Ser-15. This phosphorylation was associated with an SB203580-sensitive accumulation of p53, even in the presence of a serine phosphatase inhibitor. Accumulated p53 was localized mainly in the cytoplasm, independently of CRM1 nuclear export. In HaCaT cells, p53 was localized exclusively in the nucleus and its distribution and level were not affected by UVB or p38 inhibition. However, UVB induced an SB203580-insensitive phosphorylation on Ser-15 of mutated p53. Overall, our results suggest that, in normal human keratinocytes, protection against UVB depends on p38-mediated phosphorylation and stabilization of p53 and is tightly associated with the cytoplasmic sequestration of wild-type p53. We conclude that the p38/p53 pathway plays a key role in the adaptive response of normal human keratinocytes against UV stress.

MKK3-p38 signaling promotes apoptosis and the early inflammatory response in the obstructed mouse kidney

2007 ◽  
Vol 293 (5) ◽  
pp. F1556-F1563 ◽  
Author(s):  
Frank Y. Ma ◽  
Greg H. Tesch ◽  
Richard A. Flavell ◽  
Roger J. Davis ◽  
David J. Nikolic-Paterson
Keyword(s):  
Inflammatory Response ◽  
P38 Mapk ◽  
Renal Injury ◽  
Mapk Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Mrna Levels ◽  
Direct Role ◽  
Mitogen Activated Protein ◽  
Early Inflammatory Response ◽  
Induced Apoptosis

Activation of the p38 mitogen-activated protein kinase (MAPK) pathway induces inflammation, apoptosis, and fibrosis. However, little is known of the contribution of the upstream kinases, MMK3 and MKK6, to activation of the p38 kinase in the kidney and consequent renal injury. This study investigated the contribution of MKK3 to p38 MAPK activation and renal injury in the obstructed kidney. Groups of eight wild-type (WT) or Mkk3−/− mice underwent unilateral ureteric obstruction (UUO) and were killed 3 or 7 days later. Western blotting showed a marked increase in phospho-p38 (p-p38) MAPK in UUO WT kidney. The same trend of increased p-p38 MAPK was seen in the UUO Mkk3−/− kidney, although the actual level of p-p38 MAPK was significantly reduced compared with WT, and this could not be entirely compensated for by the increase in MKK6 expression in the Mkk3−/− kidney. Apoptosis of tubular and interstitial cells in WT UUO mice was reduced by 50% in Mkk3−/− UUO mice. Furthermore, cultured Mkk3−/− tubular epithelial cells showed resistance to H2O2-induced apoptosis, suggesting a direct role for MKK3-p38 signaling in tubular apoptosis. Upregulation of MCP-1 mRNA levels and macrophage infiltration seen on day 3 in WT UUO mice was significantly reduced in Mkk3−/− mice, but this difference was not evident by day 7. The development of renal fibrosis in Mkk3−/− UUO mice was not different from that seen in WT UUO mice. In conclusion, these studies identify discrete roles for MKK3-p38 signaling in renal cell apoptosis and the early inflammatory response in the obstructed kidney.

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